ID   HS74L_HUMAN             Reviewed;         839 AA.
AC   O95757; Q4W5M5; Q8IWA2;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   02-NOV-2010, sequence version 3.
DT   25-JAN-2012, entry version 100.
DE   RecName: Full=Heat shock 70 kDa protein 4L;
DE   AltName: Full=Heat shock 70-related protein APG-1;
DE   AltName: Full=Osmotic stress protein 94;
GN   Name=HSPA4L; Synonyms=APG1, OSP94;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT SER-211.
RC   TISSUE=Testis;
RX   MEDLINE=99453757; PubMed=10524232; DOI=10.1016/S0378-1119(99)00325-X;
RA   Nonoguchi K., Itoh K., Xue J.H., Tokuchi H., Nishiyama H., Kaneko Y.,
RA   Tatsumi K., Okuno H., Tomiwa K., Fujita J.;
RT   "Cloning of human cDNAs for Apg-1 and Apg-2, members of the Hsp110
RT   family, and chromosomal assignment of their genes.";
RL   Gene 237:21-28(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15815621; DOI=10.1038/nature03466;
RA   Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
RA   Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
RA   Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
RA   Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
RA   Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
RA   Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
RA   Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
RA   Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
RA   Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
RA   Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA   McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA   Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
RA   Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
RA   Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
RA   Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
RA   Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
RA   Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
RA   Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
RA   Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
RA   Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
RA   McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA   Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA   Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
RA   Waterston R.H., Wilson R.K.;
RT   "Generation and annotation of the DNA sequences of human chromosomes 2
RT   and 4.";
RL   Nature 434:724-731(2005).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-761, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-571, AND MASS
RP   SPECTROMETRY.
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [6]
RP   ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-272, AND MASS SPECTROMETRY.
RX   PubMed=19608861; DOI=10.1126/science.1175371;
RA   Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,
RA   Olsen J.V., Mann M.;
RT   "Lysine acetylation targets protein complexes and co-regulates major
RT   cellular functions.";
RL   Science 325:834-840(2009).
RN   [7]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA   Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
CC   -!- FUNCTION: Possesses chaperone activity in vitro where it inhibits
CC       aggregation of citrate synthase (By similarity).
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By
CC       similarity). Note=May translocate to the nucleus after heat shock
CC       (By similarity).
CC   -!- INDUCTION: By heat shock.
CC   -!- PTM: Phosphorylated upon DNA damage, probably by ATM or ATR.
CC   -!- SIMILARITY: Belongs to the heat shock protein 70 family.
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DR   EMBL; AB023421; BAA75063.1; -; mRNA.
DR   EMBL; AC093591; AAY40975.1; -; Genomic_DNA.
DR   EMBL; BC040560; AAH40560.1; -; mRNA.
DR   IPI; IPI00295485; -.
DR   RefSeq; NP_055093.2; NM_014278.2.
DR   UniGene; Hs.135554; -.
DR   ProteinModelPortal; O95757; -.
DR   SMR; O95757; 302-388.
DR   IntAct; O95757; 3.
DR   MINT; MINT-1135179; -.
DR   STRING; O95757; -.
DR   PhosphoSite; O95757; -.
DR   REPRODUCTION-2DPAGE; IPI00295485; -.
DR   PRIDE; O95757; -.
DR   Ensembl; ENST00000296464; ENSP00000296464; ENSG00000164070.
DR   Ensembl; ENST00000438626; ENSP00000390499; ENSG00000164070.
DR   GeneID; 22824; -.
DR   KEGG; hsa:22824; -.
DR   CTD; 22824; -.
DR   GeneCards; GC04P128703; -.
DR   HGNC; HGNC:17041; HSPA4L.
DR   HPA; CAB034450; -.
DR   neXtProt; NX_O95757; -.
DR   HOVERGEN; HBG047955; -.
DR   InParanoid; O95757; -.
DR   PhylomeDB; O95757; -.
DR   NextBio; 43228; -.
DR   ArrayExpress; O95757; -.
DR   Bgee; O95757; -.
DR   CleanEx; HS_HSPA4L; -.
DR   Genevestigator; O95757; -.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; ISS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; ISS:UniProtKB.
DR   GO; GO:0006986; P:response to unfolded protein; ISS:UniProtKB.
DR   InterPro; IPR018181; Heat_shock_70_CS.
DR   InterPro; IPR001023; Hsp70.
DR   InterPro; IPR013126; Hsp_70.
DR   KO; K09485; -.
DR   PANTHER; PTHR19375; Hsp70; 1.
DR   Pfam; PF00012; HSP70; 2.
DR   PRINTS; PR00301; HEATSHOCK70.
DR   PROSITE; PS00297; HSP70_1; FALSE_NEG.
DR   PROSITE; PS00329; HSP70_2; FALSE_NEG.
DR   PROSITE; PS01036; HSP70_3; 1.
PE   1: Evidence at protein level;
KW   Acetylation; ATP-binding; Chaperone; Complete proteome; Cytoplasm;
KW   Nucleotide-binding; Nucleus; Phosphoprotein; Polymorphism;
KW   Reference proteome; Stress response.
FT   CHAIN         1    839       Heat shock 70 kDa protein 4L.
FT                                /FTId=PRO_0000078280.
FT   MOD_RES      74     74       Phosphoserine (By similarity).
FT   MOD_RES     272    272       N6-acetyllysine.
FT   MOD_RES     571    571       Phosphothreonine.
FT   MOD_RES     761    761       Phosphothreonine.
FT   VARIANT     211    211       L -> S (in dbSNP:rs1380154).
FT                                /FTId=VAR_025405.
FT   VARIANT     216    216       N -> T (in dbSNP:rs12507229).
FT                                /FTId=VAR_031214.
FT   VARIANT     601    601       I -> T (in dbSNP:rs35518193).
FT                                /FTId=VAR_055966.
FT   CONFLICT    806    806       H -> R (in Ref. 1; BAA75063).
SQ   SEQUENCE   839 AA;  94512 MW;  549933AECFF4369A CRC64;
     MSVVGIDLGF LNCYIAVARS GGIETIANEY SDRCTPACIS LGSRTRAIGN AAKSQIVTNV
     RNTIHGFKKL HGRSFDDPIV QTERIRLPYE LQKMPNGSAG VKVRYLEEER PFAIEQVTGM
     LLAKLKETSE NALKKPVADC VISIPSFFTD AERRSVMAAA QVAGLNCLRL MNETTAVALA
     YGIYKQDLPP LDEKPRNVVF IDMGHSAYQV LVCAFNKGKL KVLATTFDPY LGGRNFDEAL
     VDYFCDEFKT KYKINVKENS RALLRLYQEC EKLKKLMSAN ASDLPLNIEC FMNDLDVSSK
     MNRAQFEQLC ASLLARVEPP LKAVMEQANL QREDISSIEI VGGATRIPAV KEQITKFFLK
     DISTTLNADE AVARGCALQC AILSPAFKVR EFSITDLVPY SITLRWKTSF EDGSGECEVF
     CKNHPAPFSK VITFHKKEPF ELEAFYTNLH EVPYPDARIG SFTIQNVFPQ SDGDSSKVKV
     KVRVNIHGIF SVASASVIEK QNLEGDHSDA PMETETSFKN ENKDNMDKMQ VDQEEGHQKC
     HAEHTPEEEI DHTGAKTKSA VSDKQDRLNQ TLKKGKVKSI DLPIQSSLCR QLGQDLLNSY
     IENEGKMIMQ DKLEKERNDA KNAVEEYVYD FRDRLGTVYE KFITPEDLSK LSAVLEDTEN
     WLYEDGEDQP KQVYVDKLQE LKKYGQPIQM KYMEHEERPK ALNDLGKKIQ LVMKVIEAYR
     NKDERYDHLD PTEMEKVEKC ISDAMSWLNS KMNAQNKLSL TQDPVVKVSE IVAKSKELDN
     FCNPIIYKPK PKAEVPEDKP KANSEHNGPM DGQSGTETKS DSTKDSSQHT KSSGEMEVD
//